Title : Electrochemical determination of heme-linked pKa values and the importance of using fluoride binding in heme proteins.

Pub. Date : 2013 Dec 1

PMID : 23978331






3 Functional Relationships(s)
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1 A detailed study of the pH dependence of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) reveals how protonation of the distal histidine (H64) changes the redox properties of the protein with a determined pKa of 5.3. Histidine myoglobin Equus caballus
2 A detailed study of the pH dependence of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) reveals how protonation of the distal histidine (H64) changes the redox properties of the protein with a determined pKa of 5.3. Histidine myoglobin Equus caballus
3 A detailed study of the pH dependence of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) reveals how protonation of the distal histidine (H64) changes the redox properties of the protein with a determined pKa of 5.3. Histidine myoglobin Equus caballus